› 5v2n

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a [histone H4]-L-lysine(20) = S-adenosyl-L-homocysteine + a [histone H4]-N(6)-methyl-L-lysine(20)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192509 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-lysine methyltransferase KMT5A Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NQR1 (Residues: 231-393; Coverage: 42%)
Gene names: KMT5A, PRSET7, SET07, SET8, SETD8
Sequence domains: SET domain
Structure domains: SET domain

Ligands and Environments

1 bound ligand:
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P43212
Unit cell:
a: 60.62Å b: 60.62Å c: 80.708Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.25
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Investigating Cryptic Binding Sites by Molecular Dynamics Simulations.
Kuzmanic et al. (2020)
4 more

2 mentions without citation

The dynamic conformational landscape of the protein methyltransferase SETD8.
Chen et al. (2019)
1 more